1wz9: Difference between revisions

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[[Image:1wz9.gif|left|200px]]<br /><applet load="1wz9" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1wz9.gif|left|200px]]
caption="1wz9, resolution 2.10&Aring;" />
 
'''The 2.1 A structure of a tumour suppressing serpin'''<br />
{{Structure
|PDB= 1wz9 |SIZE=350|CAPTION= <scene name='initialview01'>1wz9</scene>, resolution 2.10&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY=
|GENE= SERPINB5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''The 2.1 A structure of a tumour suppressing serpin'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1WZ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ9 OCA].  
1WZ9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ9 OCA].  


==Reference==
==Reference==
The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix., Law RH, Irving JA, Buckle AM, Ruzyla K, Buzza M, Bashtannyk-Puhalovich TA, Beddoe TC, Nguyen K, Worrall DM, Bottomley SP, Bird PI, Rossjohn J, Whisstock JC, J Biol Chem. 2005 Jun 10;280(23):22356-64. Epub 2005 Mar 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15760906 15760906]
The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix., Law RH, Irving JA, Buckle AM, Ruzyla K, Buzza M, Bashtannyk-Puhalovich TA, Beddoe TC, Nguyen K, Worrall DM, Bottomley SP, Bird PI, Rossjohn J, Whisstock JC, J Biol Chem. 2005 Jun 10;280(23):22356-64. Epub 2005 Mar 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15760906 15760906]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: tumor suppressor]]
[[Category: tumor suppressor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:39 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:03:24 2008''

Revision as of 16:03, 20 March 2008

File:1wz9.gif


PDB ID 1wz9

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands:
Gene: SERPINB5 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



The 2.1 A structure of a tumour suppressing serpin


OverviewOverview

Maspin is a serpin that acts as a tumor suppressor in a range of human cancers, including tumors of the breast and lung. Maspin is crucial for development, because homozygous loss of the gene is lethal; however, the precise physiological role of the molecule is unclear. To gain insight into the function of human maspin, we have determined its crystal structure in two similar, but non-isomorphous crystal forms, to 2.1- and 2.8-A resolution, respectively. The structure reveals that maspin adopts the native serpin fold in which the reactive center loop is expelled fully from the A beta-sheet, makes minimal contacts with the core of the molecule, and exhibits a high degree of flexibility. A buried salt bridge unique to maspin orthologues causes an unusual bulge in the region around the D and E alpha-helices, an area of the molecule demonstrated in other serpins to be important for cofactor recognition. Strikingly, the structural data reveal that maspin is able to undergo conformational change in and around the G alpha-helix, switching between an open and a closed form. This change dictates the electrostatic character of a putative cofactor binding surface and highlights this region as a likely determinant of maspin function. The high resolution crystal structure of maspin provides a detailed molecular framework to elucidate the mechanism of function of this important tumor suppressor.

About this StructureAbout this Structure

1WZ9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix., Law RH, Irving JA, Buckle AM, Ruzyla K, Buzza M, Bashtannyk-Puhalovich TA, Beddoe TC, Nguyen K, Worrall DM, Bottomley SP, Bird PI, Rossjohn J, Whisstock JC, J Biol Chem. 2005 Jun 10;280(23):22356-64. Epub 2005 Mar 10. PMID:15760906

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